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- My PDB code: 3GRS residue point: HIS467 mutation: LEU Describe why this position in your protein is important and outline the effects the mutation will have on the 3D structure and the function of your protein. (up to 50 words)tRNA charging produces a functional tRNA with an appropriate O ribose to deoxyribose ratio O lipid profile van der Waal interaction O anino acid100All tRNA molecules have poly (A) tails at their 3' end. Yesorno
- PLEASE ANSWER WHY? Some substitution mutation result in a malfunctioning protein but others do not. Why is this? N-linked glycoproteins are glycosylated co-translationally at which consensussequence? A) Asn-X-Ser B) Met -Gly -X-Asn -X-Ser C) no specific sequence D) Ser- Asn -Thr E) Cys- X-AsUsing threonyl-tRNA synthetase as an example, account for the specificity of threonyl-tRNA formation.
- In HbS, the human hemoglobin found in individuals with sickle-cell anemia, glutamic acid at position 6 in the beta chain is replaced by valine. Q.) Show that one of the glutamic acid codons can be converted to a valine codon by a single substitution mutation (i.e., by changing one letter in one codon).2) Myoclonal epilepsy and ragged red fiber disease (MERRF) is a human condition named for the ragged red fibers of skeletal muscle cells and myoclinic epilepsy in affected individuals. People with this disorder have a mutation in a mitochondrial gene for a tRNA, specifically that for lysine. Why are affected individuals are always heteroplasmic?1Need help:. draw valine-aminoacyl tRNA synthetase. Show the tRNAs and the valine amino acid. You can use the one-letter code for valine (V) and do not have to draw the amino acid structure. Label the tRNA and amino acid binding sites on the enzyme. Explain the function of valine-aminoacyl tRNA synthetase and explain why there are 20 related enzymes in every cell.
- HbS results from the substitution of valine forglutamic acid at the number 6 position in the b chainof human hemoglobin. HbC is the result of a change atthe same position in the β chain, but in this case lysinereplaces glutamic acid. Return to the genetic code table and determine whether single-nucleotide changes can account for these mutations. Then view and examine the R groups in the amino acidsglutamic acid, valine, and lysine. Describe the chemicaldifferences between the three amino acids. Predict how thechanges might alter the structure of the molecule and leadto altered hemoglobin function.13c give the codon sequences of every code on this tRNA with the anti-codon 5AAG3, could pair with including wobble matchesDescribe why this position in your protein is important and outline the effects the mutation will have on the 3D structure and the function of your protein. (up to 50 words) My PDB code: 3GRS Residue point: HIS 467 Mutation: LEU 467
